Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 217 (07 Oct 2020)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Genome polyprotein

Gene
N/A
Organism
Poliovirus type 1 (strain Mahoney)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (PubMed:2994218). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (PubMed:2994218). Capsid protein VP1 mainly forms the vertices of the capsid (PubMed:23365424). Capsid protein VP1 interacts with host cell receptor PVR to provide virion attachment to target host epithelial cells (PubMed:25631086). This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis in Hela cells and through caveolin-mediated endocytosis in brain microvascular endothelial cells (PubMed:17717529, PubMed:18191571, PubMed:17622193). Tyrosine kinases are probably involved in the entry process (PubMed:17717529). Virus binding to PVR induces increased junctional permeability and rearrangement of junctional proteins (PubMed:17717529). Modulation of endothelial tight junctions, as well as cytolytic infection of endothelial cells themselves, may result in loss of endothelial integrity which may help the virus to reach the CNS (PubMed:17717529). After binding to its receptor, the capsid undergoes conformational changes (PubMed:25631086). Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized (PubMed:25631086). Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm (PubMed:25631086).6 Publications
Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP1 and VP3 (PubMed:2994218). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (PubMed:18191571).2 Publications
Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP1 (PubMed:2994218). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (PubMed:18191571).2 Publications
Lies on the inner surface of the capsid shell (PubMed:25631086). After binding to the host receptor, the capsid undergoes conformational changes (PubMed:25631086). Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm (PubMed:25631086, PubMed:23365424).2 Publications
Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation (PubMed:7849583). Allows the capsid to remain inactive before the maturation step (PubMed:1851815).2 Publications
Cysteine protease that cleaves viral polyprotein and specific host proteins (PubMed:1649327). It is responsible for the autocatalytic cleavage between the P1 and P2 regions, which is the first cleavage occurring in the polyprotein (PubMed:1649327). Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation (PubMed:9755863). Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores including NUP98, NUP62 and NUP153 (PubMed:19789179). Counteracts stress granule formation probably by antagonizing its assembly or promoting its dissassembly (By similarity). Cleaves and inhibits host IFIH1/MDA5, thereby inhibiting the type-I IFN production and the establishment of the antiviral state (PubMed:24390337). Cleaves and inhibits host MAVS, thereby inhibiting the type-I IFN production and the establishment of the antiviral state (PubMed:24390337).By similarity4 Publications
Plays an essential role in the virus replication cycle by acting as a viroporin (PubMed:21835803). Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (PubMed:9151862).2 Publications
Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities (PubMed:7730315, PubMed:19520852, PubMed:8385138, PubMed:30231078). May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3 (PubMed:22761387).5 Publications
Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity.1 Publication
Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction (PubMed:17079330, PubMed:15914217). This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (PubMed:17079330, PubMed:15914217). Plays an essential role in viral RNA replication by recruiting ACBD3 and PI4KB at the viral replication sites, thereby allowing the formation of the rearranged membranous structures where viral replication takes place (Probable) (PubMed:31381608).1 Publication3 Publications
Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA (PubMed:12502805, PubMed:20441784, PubMed:16840321, PubMed:209034, PubMed:6250717). VPg is uridylylated prior to priming replication into VPg-pUpU (PubMed:12502805, PubMed:20441784, PubMed:16840321). The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome (PubMed:12502805, PubMed:16840321). Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (PubMed:22908287). During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions (PubMed:22908287).6 Publications
Involved in the viral replication complex and viral polypeptide maturation (PubMed:1331532, PubMed:10666252). It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C (PubMed:1331532). Protein 3CD binds to the 5'UTR of the viral genome (PubMed:10666252).2 Publications
Major viral protease that mediates proteolytic processing of the polyprotein (PubMed:8097606). Cleaves host EIF5B, contributing to host translation shutoff (PubMed:18572216). Cleaves also host PABPC1, contributing to host translation shutoff (PubMed:18632855). Cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production (PubMed:24390337).4 Publications
Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss+RNA genomes are either translated, replicated or encapsidated.1 Publication

Caution

Has been proposed to interact with host LIS1/NUF (PubMed:16138011), but this has not been confirmed by other studies (PubMed:21345960).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.1 Publication EC:3.4.22.29
  • Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.PROSITE-ProRule annotation1 Publication EC:3.4.22.28

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

RNA-directed RNA polymerase:
Mg2+1 PublicationNote: Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (PubMed:21148772). The magnesium ions are not prebound but only present for catalysis (PubMed:21148772). Requires the presence of 3CDpro or 3CPro (By similarity).By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Replication or transcription is subject to high level of random mutations by the nucleotide analog ribavirin.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

For protein 2C ATPase activity.1 Publication
  1. KM=642 µM for ATP1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei901For protease 2A activity1 Publication1
    Active sitei919For protease 2A activity1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi936Zinc; structural1 Publication1
    Metal bindingi938Zinc; structural1 Publication1
    Active sitei990For protease 2A activity1 Publication1
    Metal bindingi996Zinc; structural1 Publication1
    Metal bindingi998Zinc; via pros nitrogen; structural1 Publication1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1152Involved in the interaction with host RTN3By similarity1
    Metal bindingi1396Zinc1 Publication1
    Metal bindingi1399Zinc1 Publication1
    Metal bindingi1408Zinc1 Publication1
    Metal bindingi1413Zinc1 Publication1
    Active sitei1605For protease 3C activityPROSITE-ProRule annotation1
    Active sitei1636For protease 3C activityPROSITE-ProRule annotation1 Publication1
    Active sitei1712For protease 3C activityPROSITE-ProRule annotation1 Publication1
    Metal bindingi1981Magnesium 1; catalytic; for RdRp activity1 Publication1
    Metal bindingi1981Magnesium 2; catalytic; for RdRp activity1 Publication1
    Metal bindingi2076Magnesium 1; catalytic; for RdRp activity1 Publication1 Publication1
    Metal bindingi2076Magnesium 2; catalytic; for RdRp activity1 Publication1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1256 – 1263ATPPROSITE-ProRule annotation8
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri1396 – 1413C4-type1 PublicationAdd BLAST18

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHelicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel
    Biological processActivation of host autophagy by virus, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host MAVS by virus, Inhibition of host MDA5 by virus, Inhibition of host mRNA nuclear export by virus, Inhibition of host RIG-I by virus, Inhibition of host RLR pathway by virus, Ion transport, Pore-mediated penetration of viral genome into host cell, Transport, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    C03.001

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Genome polyprotein
    Cleaved into the following 17 chains:
    Alternative name(s):
    VP4-VP2
    Alternative name(s):
    P1A
    Virion protein 4
    Alternative name(s):
    P1B
    Virion protein 2
    Alternative name(s):
    P1C
    Virion protein 3
    Alternative name(s):
    P1D
    Virion protein 1
    Protease 2A (EC:3.4.22.291 Publication)
    Short name:
    P2A
    Alternative name(s):
    Picornain 2A
    Protein 2A
    Protein 2B
    Short name:
    P2B
    Protein 2C (EC:3.6.1.154 Publications)
    Short name:
    P2C
    Protein 3A
    Short name:
    P3A
    Alternative name(s):
    Protein 3B
    Short name:
    P3B
    Protein 3CD (EC:3.4.22.28)
    Protease 3CPROSITE-ProRule annotation (EC:3.4.22.28PROSITE-ProRule annotation1 Publication)
    Alternative name(s):
    Picornain 3CPROSITE-ProRule annotation
    Short name:
    P3CPROSITE-ProRule annotation
    RNA-directed RNA polymerasePROSITE-ProRule annotation (EC:2.7.7.48PROSITE-ProRule annotation)
    Short name:
    RdRp
    Alternative name(s):
    3D polymerase
    Short name:
    3Dpol
    Protein 3D
    Short name:
    3D
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPoliovirus type 1 (strain Mahoney)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri12081 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesRiboviriaOrthornaviraePisuviricotaPisoniviricetesPicornaviralesPicornaviridaeEnterovirusEnterovirus C
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiHomo sapiens (Human) [TaxID: 9606]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000356 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome
    • UP000149468 Componenti: Genome
    • UP000138192 Componenti: Genome

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini2 – 1520CytoplasmicSequence analysisAdd BLAST1519
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei1521 – 1536Sequence analysisAdd BLAST16
    Topological domaini1537 – 2209CytoplasmicSequence analysisAdd BLAST673

    GO - Cellular componenti

    Keywords - Cellular componenti

    Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, Membrane, T=pseudo3 icosahedral capsid protein, Virion

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi2G → A: 100% loss of myristoylation. Impaired viral assembly. 1 Publication1
    Mutagenesisi3A → D: 50% loss of myristoylation. Severe reduction in specific infectivity. 1 Publication1
    Mutagenesisi3A → G, L or V: No effect on myristoylation and virus growth. 1 Publication1
    Mutagenesisi3A → H: No effect on myristoylation. Severe reduction in specific infectivity. 1 Publication1
    Mutagenesisi264H → G or T: Complete loss of VP0 cleavage. 1 Publication1
    Mutagenesisi901H → A: Complete loss of catalytic activity. 1 Publication1
    Mutagenesisi919D → A: Complete loss of catalytic activity. 1 Publication1
    Mutagenesisi936C → S: Complete loss of autocatalytic activity of protease 2A. Complete loss of polyprotein cleavage. 1 Publication1
    Mutagenesisi938C → S, N or T: Complete loss of autocatalytic activity of protease 2A. Complete loss of polyprotein cleavage. 1 Publication1
    Mutagenesisi945C → N or S: Almost no effect on the autocatalytic activity of protease 2A. Almost no effect on polyprotein cleavage. 1 Publication1
    Mutagenesisi990C → A: Complete loss of catalytic activity. 1 Publication1
    Mutagenesisi990C → S: 90% loss of catalytic activity. 1 Publication1
    Mutagenesisi996C → H, P, S or Y: Complete loss of autocatalytic activity of protease 2A. Complete loss of polyprotein cleavage. 1 Publication1
    Mutagenesisi997H → R: No effect on catalytic activity. 1 Publication1
    Mutagenesisi998H → A: 95% loss of catalytic activity. 1 Publication1
    Mutagenesisi998H → Q: Complete loss of autocatalytic activity of protease 2A. Complete loss of polyprotein cleavage. 1 Publication1
    Mutagenesisi1262K → A: Complete loss of protein 2C ATPase activity. 1 Publication1
    Mutagenesisi1268L → R: 95% loss of protein 2C ATPase activity. 1 Publication1
    Mutagenesisi1272A → R: 80% loss of protein 2C ATPase activity. 1 Publication1
    Mutagenesisi1304D → A: Complete loss of protein 2C ATPase activity. 1 Publication1
    Mutagenesisi1350N → A: Complete loss of protein 2C ATPase activity. 1 Publication1
    Mutagenesisi1368R → A: Complete loss of protein 2C ATPase activity. 1 Publication1
    Mutagenesisi1396C → A: 78% loss of 2C ATPase activity. 1 Publication1
    Mutagenesisi1399C → A: 30% loss of 2C ATPase activity. 1 Publication1
    Mutagenesisi1405F → R: 80% loss of protein 2C ATPase activity. 1 Publication1
    Mutagenesisi1408C → A: 87% loss of 2C ATPase activity. 1 Publication1
    Mutagenesisi1411L → R: 80% loss of protein 2C ATPase activity. 1 Publication1
    Mutagenesisi1413C → A: 90% loss of 2C ATPase activity. 1 Publication1
    Mutagenesisi1450C → A: No effect on 2C ATPase activity and on oligomerization. 1 Publication1
    Mutagenesisi1451M → A: 90% loss of 2C ATPase activity. 1 Publication1
    Mutagenesisi1454L → A: Complete loss of 2C ATPase activity. 1 Publication1
    Mutagenesisi1455F → A: Almost complete loss of 2C ATPase activity. 1 Publication1
    Mutagenesisi1636E → Q: Complete loss of catalytic activity; when associated with S-1712. 1 Publication1
    Mutagenesisi1712C → S: Complete loss of catalytic activity; when associated with Q-1636. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL5127

    Drug and drug target database

    More...
    DrugBanki
    DB08014, (METHYLPYRIDAZINE PIPERIDINE BUTYLOXYPHENYL)ETHYLACETATE
    DB08013, (METHYLPYRIDAZINE PIPERIDINE PROPYLOXYPHENYL)ETHYLACETATE
    DB04137, Guanosine-5'-Triphosphate
    DB08231, Myristic acid
    DB08012, Pirodavir
    DB03963, S-(Dimethylarsenic)Cysteine
    DB03203, Sphingosine

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; by host1 Publication
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004246862 – 2209Genome polyproteinAdd BLAST2208
    ChainiPRO_00004246872 – 881P1Add BLAST880
    ChainiPRO_00004246882 – 341Capsid protein VP0Add BLAST340
    ChainiPRO_00000400802 – 69Capsid protein VP4Add BLAST68
    ChainiPRO_000004008170 – 341Capsid protein VP2Add BLAST272
    ChainiPRO_0000040082342 – 579Capsid protein VP3Add BLAST238
    ChainiPRO_0000040083580 – 881Capsid protein VP1Add BLAST302
    ChainiPRO_0000424689882 – 1456P2Add BLAST575
    ChainiPRO_0000040084882 – 1030Protease 2AAdd BLAST149
    ChainiPRO_00000400851031 – 1127Protein 2BAdd BLAST97
    ChainiPRO_00000400861128 – 1456Protein 2CAdd BLAST329
    ChainiPRO_00004246901457 – 2209P3Add BLAST753
    ChainiPRO_00004246911457 – 1565Protein 3ABAdd BLAST109
    ChainiPRO_00004246921457 – 1543Protein 3AAdd BLAST87
    ChainiPRO_00000400881544 – 1565Viral protein genome-linkedAdd BLAST22
    ChainiPRO_00004246931566 – 2209Protein 3CDAdd BLAST644
    ChainiPRO_00000400891566 – 1748Protease 3CAdd BLAST183
    ChainiPRO_00000400901749 – 2209RNA-directed RNA polymeraseAdd BLAST461

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine; by host3 Publications1
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1546O-(5'-phospho-RNA)-tyrosine1 Publication1
    Modified residuei1546O-UMP-tyrosine; transient2 Publications1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins.1 Publication
    Myristoylation is required for the formation of pentamers during virus assembly (PubMed:1850017, PubMed:1851815). Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion.2 Publications
    During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion.1 Publication
    Myristoylation is required during RNA encapsidation and formation of the mature virus particle.1 Publication
    VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication.2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei69 – 70Cleavage; by autolysis1 Publication2
    Sitei341 – 342Cleavage; by protease 3CBy similarity2
    Sitei579 – 580Cleavage; by protease 3CBy similarity2
    Sitei881 – 882Cleavage; by autolysisBy similarity2
    Sitei1030 – 1031Cleavage; by protease 3CBy similarity2
    Sitei1127 – 1128Cleavage; by protease 3CBy similarity2
    Sitei1456 – 1457Cleavage; by protease 3CBy similarity2
    Sitei1543 – 1544Cleavage; by protease 3CBy similarity2
    Sitei1565 – 1566Cleavage; by protease 3CBy similarity2
    Sitei1748 – 1749Cleavage; by protease 3CBy similarity2

    Keywords - PTMi

    Autocatalytic cleavage, Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P03300

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P03300

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers.

    1 Publication

    Interacts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers (PubMed:2994218). Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid (PubMed:2994218).

    Interacts with capsid protein VP2, capsid protein VP3 and capsid protein VP4 following cleavage of capsid protein VP0 (PubMed:10618374, PubMed:2994218).

    Interacts with human PVR (PubMed:10618374).

    2 Publications

    Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid.

    1 Publication

    Interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers (PubMed:2994218). Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid (PubMed:2994218).

    Interacts with capsid protein VP4 in the mature capsid (PubMed:2994218).

    Interacts with protein 2C; this interaction may be important for virion morphogenesis (PubMed:20865167).

    2 Publications

    Interacts with capsid protein VP1 and capsid protein VP3.

    1 Publication

    Homodimer.

    By similarity

    Homohexamer; forms a hexameric ring structure with 6-fold symmetry characteristic of AAA+ ATPases (Probable).

    Interacts (via N-terminus) with host RTN3 (via reticulon domain); this interaction is important for viral replication (PubMed:17182608).

    Interacts with capsid protein VP3; this interaction may be important for virion morphogenesis (PubMed:20865167).

    2 Publications2 Publications

    Interacts with protein 3CD.

    1 Publication

    Homodimer (PubMed:31381608, PubMed:12823963).

    Interacts with host GBF1 (PubMed:17005635, PubMed:21345960).

    Interacts (via GOLD domain) with host ACBD3 (via GOLD domain); this interaction allows the formation of a viral protein 3A/ACBD3 heterotetramer with a 2:2 stoichiometry, which will stimulate the recruitment of host PI4KB in order to synthesize PI4P at the viral RNA replication sites (PubMed:22258260, PubMed:31381608).

    5 Publications

    Interacts with RNA-directed RNA polymerase.

    1 Publication

    Interacts with protein 3AB and with RNA-directed RNA polymerase.

    1 Publication

    Interacts with Viral protein genome-linked and with protein 3CD.

    1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Hide details

    Protein-protein interaction databases

    The Eukaryotic Linear Motif resource for Functional Sites in Proteins

    More...
    ELMi
    P03300

    Protein interaction database and analysis system

    More...
    IntActi
    P03300, 4 interactors

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P03300

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    12209
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Biological Magnetic Resonance Data Bank

    More...
    BMRBi
    P03300

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P03300

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P03300

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1232 – 1388SF3 helicasePROSITE-ProRule annotationAdd BLAST157
    Domaini1566 – 1744Peptidase C3PROSITE-ProRule annotationAdd BLAST179
    Domaini1975 – 2090RdRp catalyticPROSITE-ProRule annotationAdd BLAST116

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni580 – 600Amphipatic alpha-helixSequence analysisAdd BLAST21
    Regioni1128 – 1266Oligomerization1 PublicationAdd BLAST139
    Regioni1128 – 1200Membrane-binding1 PublicationAdd BLAST73
    Regioni1149 – 1153RNA-binding1 Publication5
    Regioni1440 – 1447RNA-binding1 Publication8
    Regioni1451 – 1456Oligomerization1 Publication6
    Regioni1457 – 1479DisorderedSequence analysisAdd BLAST23

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The N-terminus has membrane-binding (PubMed:9696129). The N-terminus also displays RNA-binding properties (PubMed:7730315). The N-terminus is involved in oligomerization (PubMed:19520852). The central part contains an ATPase domain and a C4-type zinc-finger (PubMed:30231078). The C-terminus is involved in RNA-binding (PubMed:7730315). The extreme C-terminus contains a region involved in oligomerization (PubMed:30231078).4 Publications

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the picornaviruses polyprotein family.Curated

    Zinc finger

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Zinc fingeri1396 – 1413C4-type1 PublicationAdd BLAST18

    Keywords - Domaini

    Repeat, Zinc-finger

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00205, rhv_like, 3 hits

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.10.870, 1 hit
    2.40.10.10, 4 hits
    2.60.120.20, 3 hits
    3.30.70.270, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR043502, DNA/RNA_pol_sf
    IPR000605, Helicase_SF3_ssDNA/RNA_vir
    IPR014759, Helicase_SF3_ssRNA_vir
    IPR027417, P-loop_NTPase
    IPR014838, P3A
    IPR036203, P3A_soluble_dom
    IPR000081, Peptidase_C3
    IPR000199, Peptidase_C3A/C3B_picornavir
    IPR009003, Peptidase_S1_PA
    IPR043504, Peptidase_S1_PA_chymotrypsin
    IPR003138, Pico_P1A
    IPR002527, Pico_P2B
    IPR001676, Picornavirus_capsid
    IPR043128, Rev_trsase/Diguanyl_cyclase
    IPR033703, Rhv-like
    IPR001205, RNA-dir_pol_C
    IPR007094, RNA-dir_pol_PSvirus
    IPR029053, Viral_coat

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF08727, P3A, 1 hit
    PF00548, Peptidase_C3, 1 hit
    PF02226, Pico_P1A, 1 hit
    PF00947, Pico_P2A, 1 hit
    PF01552, Pico_P2B, 1 hit
    PF00680, RdRP_1, 1 hit
    PF00073, Rhv, 3 hits
    PF00910, RNA_helicase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF50494, SSF50494, 2 hits
    SSF52540, SSF52540, 1 hit
    SSF56672, SSF56672, 1 hit
    SSF89043, SSF89043, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51874, PCV_3C_PRO, 1 hit
    PS50507, RDRP_SSRNA_POS, 1 hit
    PS51218, SF3_HELICASE_2, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P03300-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYRDSASNA ASKQDFSQDP
    60 70 80 90 100
    SKFTEPIKDV LIKTAPMLNS PNIEACGYSD RVLQLTLGNS TITTQEAANS
    110 120 130 140 150
    VVAYGRWPEY LRDSEANPVD QPTEPDVAAC RFYTLDTVSW TKESRGWWWK
    160 170 180 190 200
    LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ CNASKFHQGA LGVFAVPEMC
    210 220 230 240 250
    LAGDSNTTTM HTSYQNANPG EKGGTFTGTF TPDNNQTSPA RRFCPVDYLL
    260 270 280 290 300
    GNGTLLGNAF VFPHQIINLR TNNCATLVLP YVNSLSIDSM VKHNNWGIAI
    310 320 330 340 350
    LPLAPLNFAS ESSPEIPITL TIAPMCCEFN GLRNITLPRL QGLPVMNTPG
    360 370 380 390 400
    SNQYLTADNF QSPCALPEFD VTPPIDIPGE VKNMMELAEI DTMIPFDLSA
    410 420 430 440 450
    TKKNTMEMYR VRLSDKPHTD DPILCLSLSP ASDPRLSHTM LGEILNYYTH
    460 470 480 490 500
    WAGSLKFTFL FCGFMMATGK LLVSYAPPGA DPPKKRKEAM LGTHVIWDIG
    510 520 530 540 550
    LQSSCTMVVP WISNTTYRQT IDDSFTEGGY ISVFYQTRIV VPLSTPREMD
    560 570 580 590 600
    ILGFVSACND FSVRLLRDTT HIEQKALAQG LGQMLESMID NTVRETVGAA
    610 620 630 640 650
    TSRDALPNTE ASGPTHSKEI PALTAVETGA TNPLVPSDTV QTRHVVQHRS
    660 670 680 690 700
    RSESSIESFF ARGACVTIMT VDNPASTTNK DKLFAVWKIT YKDTVQLRRK
    710 720 730 740 750
    LEFFTYSRFD MELTFVVTAN FTETNNGHAL NQVYQIMYVP PGAPVPEKWD
    760 770 780 790 800
    DYTWQTSSNP SIFYTYGTAP ARISVPYVGI SNAYSHFYDG FSKVPLKDQS
    810 820 830 840 850
    AALGDSLYGA ASLNDFGILA VRVVNDHNPT KVTSKIRVYL KPKHIRVWCP
    860 870 880 890 900
    RPPRAVAYYG PGVDYKDGTL TPLSTKDLTT YGFGHQNKAV YTAGYKICNY
    910 920 930 940 950
    HLATQDDLQN AVNVMWSRDL LVTESRAQGT DSIARCNCNA GVYYCESRRK
    960 970 980 990 1000
    YYPVSFVGPT FQYMEANNYY PARYQSHMLI GHGFASPGDC GGILRCHHGV
    1010 1020 1030 1040 1050
    IGIITAGGEG LVAFSDIRDL YAYEEEAMEQ GITNYIESLG AAFGSGFTQQ
    1060 1070 1080 1090 1100
    ISDKITELTN MVTSTITEKL LKNLIKIISS LVIITRNYED TTTVLATLAL
    1110 1120 1130 1140 1150
    LGCDASPWQW LRKKACDVLE IPYVIKQGDS WLKKFTEACN AAKGLEWVSN
    1160 1170 1180 1190 1200
    KISKFIDWLK EKIIPQARDK LEFVTKLRQL EMLENQISTI HQSCPSQEHQ
    1210 1220 1230 1240 1250
    EILFNNVRWL SIQSKRFAPL YAVEAKRIQK LEHTINNYIQ FKSKHRIEPV
    1260 1270 1280 1290 1300
    CLLVHGSPGT GKSVATNLIA RAIAERENTS TYSLPPDPSH FDGYKQQGVV
    1310 1320 1330 1340 1350
    IMDDLNQNPD GADMKLFCQM VSTVEFIPPM ASLEEKGILF TSNYVLASTN
    1360 1370 1380 1390 1400
    SSRISPPTVA HSDALARRFA FDMDIQVMNE YSRDGKLNMA MATEMCKNCH
    1410 1420 1430 1440 1450
    QPANFKRCCP LVCGKAIQLM DKSSRVRYSI DQITTMIINE RNRRSNIGNC
    1460 1470 1480 1490 1500
    MEALFQGPLQ YKDLKIDIKT SPPPECINDL LQAVDSQEVR DYCEKKGWIV
    1510 1520 1530 1540 1550
    NITSQVQTER NINRAMTILQ AVTTFAAVAG VVYVMYKLFA GHQGAYTGLP
    1560 1570 1580 1590 1600
    NKKPNVPTIR TAKVQGPGFD YAVAMAKRNI VTATTSKGEF TMLGVHDNVA
    1610 1620 1630 1640 1650
    ILPTHASPGE SIVIDGKEVE ILDAKALEDQ AGTNLEITII TLKRNEKFRD
    1660 1670 1680 1690 1700
    IRPHIPTQIT ETNDGVLIVN TSKYPNMYVP VGAVTEQGYL NLGGRQTART
    1710 1720 1730 1740 1750
    LMYNFPTRAG QCGGVITCTG KVIGMHVGGN GSHGFAAALK RSYFTQSQGE
    1760 1770 1780 1790 1800
    IQWMRPSKEV GYPIINAPSK TKLEPSAFHY VFEGVKEPAV LTKNDPRLKT
    1810 1820 1830 1840 1850
    DFEEAIFSKY VGNKITEVDE YMKEAVDHYA GQLMSLDINT EQMCLEDAMY
    1860 1870 1880 1890 1900
    GTDGLEALDL STSAGYPYVA MGKKKRDILN KQTRDTKEMQ KLLDTYGINL
    1910 1920 1930 1940 1950
    PLVTYVKDEL RSKTKVEQGK SRLIEASSLN DSVAMRMAFG NLYAAFHKNP
    1960 1970 1980 1990 2000
    GVITGSAVGC DPDLFWSKIP VLMEEKLFAF DYTGYDASLS PAWFEALKMV
    2010 2020 2030 2040 2050
    LEKIGFGDRV DYIDYLNHSH HLYKNKTYCV KGGMPSGCSG TSIFNSMINN
    2060 2070 2080 2090 2100
    LIIRTLLLKT YKGIDLDHLK MIAYGDDVIA SYPHEVDASL LAQSGKDYGL
    2110 2120 2130 2140 2150
    TMTPADKSAT FETVTWENVT FLKRFFRADE KYPFLIHPVM PMKEIHESIR
    2160 2170 2180 2190 2200
    WTKDPRNTQD HVRSLCLLAW HNGEEEYNKF LAKIRSVPIG RALLLPEYST

    LYRRWLDSF
    Length:2,209
    Mass (Da):246,540
    Last modified:January 23, 2007 - v3
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDF1754F87F2E97D6
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti242 – 264RFCPV…FVFPH → SSARWITSLEMARCWGMPLC SA in CAA24446 (PubMed:6272282).CuratedAdd BLAST23
    Sequence conflicti287I → L in CAA24446 (PubMed:6272282).Curated1
    Sequence conflicti309A → V in CAA24446 (PubMed:6272282).Curated1
    Sequence conflicti420 – 422DDP → AAS in CAA24446 (PubMed:6272282).Curated3
    Sequence conflicti464F → S in CAA24446 (PubMed:6272282).Curated1
    Sequence conflicti464F → S in AMS03992 (Ref. 3) Curated1
    Sequence conflicti515T → S in CAA24446 (PubMed:6272282).Curated1
    Sequence conflicti674P → S in AMS03992 (Ref. 3) Curated1
    Sequence conflicti855 – 856AV → QL in CAA24446 (PubMed:6272282).Curated2
    Sequence conflicti906D → E in AMS03992 (Ref. 3) Curated1
    Sequence conflicti972A → V in CAA24446 (PubMed:6272282).Curated1
    Sequence conflicti985A → E in CAA24446 (PubMed:6272282).Curated1
    Sequence conflicti1052S → G in AMS03992 (Ref. 3) Curated1
    Sequence conflicti1140 – 1141NA → QR in CAA24446 (PubMed:6272282).Curated2
    Sequence conflicti1619V → A in CAA24446 (PubMed:6272282).Curated1
    Sequence conflicti1626 – 1627AL → VF in CAA24446 (PubMed:6272282).Curated2
    Sequence conflicti1635L → F in CAA24446 (PubMed:6272282).Curated1
    Sequence conflicti1682G → R in CAA24446 (PubMed:6272282).Curated1
    Sequence conflicti1722 – 1730VIGMHVGGN → SSGCMLVD in CAA24446 (PubMed:6272282).Curated9
    Sequence conflicti1743Y → L in CAA24446 (PubMed:6272282).Curated1
    Sequence conflicti1752Q → P in CAA24446 (PubMed:6272282).Curated1
    Sequence conflicti1759 – 1760EV → DA in CAA24446 (PubMed:6272282).Curated2
    Sequence conflicti1840T → I in CAA24446 (PubMed:6272282).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    V01149 Genomic RNA Translation: CAA24461.1
    V01148 Genomic RNA Translation: CAA24446.1
    KU866422 Genomic RNA Translation: AMS03992.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A03898, GNNY2P
    A93258, GNNY1P

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_041277.1, NC_002058.3

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    919920

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    vg:919920

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    Virus Particle ExploreR db

    Icosahedral capsid structure associated with cellular receptor

    Virus Particle ExploreR db

    Icosahedral capsid structure associated with cellular receptor

    Virus Particle ExploreR db

    Icosahedral capsid structure in complex with R80633, an inhibitor of viral replication

    Virus Particle ExploreR db

    Icosahedral capsid structure in complex with R77975, an inhibitor of viral replication

    Virus Particle ExploreR db

    Icosahedral empty capsid structure

    Virus Particle ExploreR db

    Icosahedral capsid structure complexed with R78206

    Virus Particle ExploreR db

    Icosahedral capsid structure

    Virus Particle ExploreR db

    Icosahedral capsid structure of 135S cell entry intermediate

    Virus Particle ExploreR db

    Icosahedral capsid structure

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    V01149 Genomic RNA Translation: CAA24461.1
    V01148 Genomic RNA Translation: CAA24446.1
    KU866422 Genomic RNA Translation: AMS03992.1
    PIRiA03898, GNNY2P
    A93258, GNNY1P
    RefSeqiNP_041277.1, NC_002058.3

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1AL2X-ray2.901580-881[»]
    270-341[»]
    3342-579[»]
    42-69[»]
    1AR6X-ray2.901580-881[»]
    270-341[»]
    3342-579[»]
    42-69[»]
    1AR7X-ray2.901580-881[»]
    270-341[»]
    3342-579[»]
    42-69[»]
    1AR8X-ray2.901580-881[»]
    270-341[»]
    3342-579[»]
    42-69[»]
    1AR9X-ray2.901580-881[»]
    270-341[»]
    3342-579[»]
    42-69[»]
    1ASJX-ray2.901580-881[»]
    270-341[»]
    3342-579[»]
    42-69[»]
    1DGIelectron microscopy22.001599-881[»]
    274-341[»]
    3342-576[»]
    42-69[»]
    1FPTX-ray3.00P665-682[»]
    1HXSX-ray2.201580-881[»]
    270-341[»]
    3342-578[»]
    42-69[»]
    1L1NX-ray2.10A/B1566-1748[»]
    1NG7NMR-A/B1457-1515[»]
    1NN8electron microscopy15.001580-881[»]
    270-341[»]
    3342-576[»]
    42-69[»]
    1PO1X-ray2.901580-881[»]
    270-341[»]
    3342-579[»]
    42-69[»]
    1PO2X-ray2.901580-881[»]
    270-341[»]
    3342-579[»]
    42-69[»]
    1POVX-ray2.8002-341[»]
    1580-881[»]
    3342-579[»]
    1RA6X-ray2.00A1749-2209[»]
    1RA7X-ray2.35A1749-2209[»]
    1RAJX-ray2.50A1817-2209[»]
    1RDRX-ray2.40A1749-2209[»]
    1TQLX-ray2.30A1749-2209[»]
    1VBDX-ray2.901580-881[»]
    270-341[»]
    3342-579[»]
    42-69[»]
    1XYRelectron microscopy11.001650-881[»]
    297-333[»]
    3391-572[»]
    5342-353[»]
    6355-390[»]
    782-95[»]
    8621-631[»]
    2BBLNMR-A1544-1565[»]
    2BBPNMR-A1544-1565[»]
    2IJDX-ray3.401/21566-2208[»]
    2IJFX-ray3.00A1749-2208[»]
    2ILYX-ray2.60A1749-2208[»]
    2ILZX-ray2.50A1749-2208[»]
    2IM0X-ray2.25A1749-2208[»]
    2IM1X-ray2.50A1749-2208[»]
    2IM2X-ray2.35A1749-2208[»]
    2IM3X-ray2.60A1749-2208[»]
    2PLVX-ray2.881580-881[»]
    270-341[»]
    3342-579[»]
    42-69[»]
    3EPCelectron microscopy8.001599-881[»]
    274-341[»]
    3342-576[»]
    42-69[»]
    3IYBelectron microscopy10.001647-881[»]
    3342-572[»]
    497-341[»]
    3IYCelectron microscopy-1647-881[»]
    497-341[»]
    3J3Oelectron microscopy11.101580-881[»]
    270-341[»]
    3342-579[»]
    42-69[»]
    3J3Pelectron microscopy9.101580-881[»]
    270-341[»]
    3342-579[»]
    3J48electron microscopy5.501580-881[»]
    270-341[»]
    3342-579[»]
    3J8Felectron microscopy3.701580-881[»]
    270-341[»]
    3342-579[»]
    42-69[»]
    3J9Felectron microscopy9.001580-881[»]
    270-341[»]
    3342-579[»]
    42-69[»]
    3JBCelectron microscopy5.601580-881[»]
    270-341[»]
    3342-578[»]
    42-69[»]
    3JBDelectron microscopy4.701580-881[»]
    270-341[»]
    3342-578[»]
    42-69[»]
    3JBEelectron microscopy4.201580-881[»]
    270-341[»]
    3342-578[»]
    42-69[»]
    3JBFelectron microscopy4.601580-881[»]
    270-341[»]
    3342-578[»]
    42-69[»]
    3JBGelectron microscopy3.801580-881[»]
    270-341[»]
    3342-578[»]
    42-69[»]
    3OL7X-ray2.70A/E/I/M1749-2209[»]
    4DCDX-ray1.69A1566-1748[»]
    4K4SX-ray2.40A/E1749-2209[»]
    4K4TX-ray2.75A/E1749-2209[»]
    4K4UX-ray2.85A/E1749-2209[»]
    4K4VX-ray2.63A/E1749-2209[»]
    4K4WX-ray2.69A/E1749-2209[»]
    4NLOX-ray2.20A1749-2209[»]
    4NLPX-ray2.20A1749-2209[»]
    4NLQX-ray2.30A1749-2209[»]
    4NLRX-ray2.00A1749-2209[»]
    4NLSX-ray2.00A1749-2209[»]
    4NLTX-ray2.50A1749-2209[»]
    4NLUX-ray2.10A1749-2209[»]
    4NLVX-ray2.30A1749-2209[»]
    4NLWX-ray2.10A1749-2209[»]
    4NLXX-ray2.60A1749-2209[»]
    4NLYX-ray2.30A1749-2209[»]
    4R0EX-ray3.00A1749-2209[»]
    5KTZelectron microscopy4.301636-858[»]
    270-338[»]
    3342-572[»]
    5KU0electron microscopy4.201636-858[»]
    270-338[»]
    3342-572[»]
    5KU2electron microscopy4.501650-858[»]
    270-337[»]
    3342-571[»]
    5KWLelectron microscopy4.501650-858[»]
    270-337[»]
    3342-571[»]
    5Z3QX-ray2.54A/B/C/D/E/H1243-1456[»]
    6HLVX-ray2.50B1457-1514[»]
    6P9Oelectron microscopy2.901580-881[»]
    270-341[»]
    6P9Welectron microscopy3.201580-881[»]
    270-341[»]
    6PSZelectron microscopy3.201580-881[»]
    270-341[»]
    BMRBiP03300
    SMRiP03300
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    ELMiP03300
    IntActiP03300, 4 interactors

    Chemistry databases

    BindingDBiP03300
    ChEMBLiCHEMBL5127
    DrugBankiDB08014, (METHYLPYRIDAZINE PIPERIDINE BUTYLOXYPHENYL)ETHYLACETATE
    DB08013, (METHYLPYRIDAZINE PIPERIDINE PROPYLOXYPHENYL)ETHYLACETATE
    DB04137, Guanosine-5'-Triphosphate
    DB08231, Myristic acid
    DB08012, Pirodavir
    DB03963, S-(Dimethylarsenic)Cysteine
    DB03203, Sphingosine

    Protein family/group databases

    MEROPSiC03.001

    PTM databases

    iPTMnetiP03300

    Proteomic databases

    PRIDEiP03300

    Protocols and materials databases

    ABCD curated depository of sequenced antibodies

    More...
    ABCDi
    P03300, 10 sequenced antibodies

    Genome annotation databases

    GeneIDi919920
    KEGGivg:919920

    Miscellaneous databases

    EvolutionaryTraceiP03300

    Family and domain databases

    CDDicd00205, rhv_like, 3 hits
    Gene3Di1.10.10.870, 1 hit
    2.40.10.10, 4 hits
    2.60.120.20, 3 hits
    3.30.70.270, 1 hit
    InterProiView protein in InterPro
    IPR043502, DNA/RNA_pol_sf
    IPR000605, Helicase_SF3_ssDNA/RNA_vir
    IPR014759, Helicase_SF3_ssRNA_vir
    IPR027417, P-loop_NTPase
    IPR014838, P3A
    IPR036203, P3A_soluble_dom
    IPR000081, Peptidase_C3
    IPR000199, Peptidase_C3A/C3B_picornavir
    IPR009003, Peptidase_S1_PA
    IPR043504, Peptidase_S1_PA_chymotrypsin
    IPR003138, Pico_P1A
    IPR002527, Pico_P2B
    IPR001676, Picornavirus_capsid
    IPR043128, Rev_trsase/Diguanyl_cyclase
    IPR033703, Rhv-like
    IPR001205, RNA-dir_pol_C
    IPR007094, RNA-dir_pol_PSvirus
    IPR029053, Viral_coat
    PfamiView protein in Pfam
    PF08727, P3A, 1 hit
    PF00548, Peptidase_C3, 1 hit
    PF02226, Pico_P1A, 1 hit
    PF00947, Pico_P2A, 1 hit
    PF01552, Pico_P2B, 1 hit
    PF00680, RdRP_1, 1 hit
    PF00073, Rhv, 3 hits
    PF00910, RNA_helicase, 1 hit
    SUPFAMiSSF50494, SSF50494, 2 hits
    SSF52540, SSF52540, 1 hit
    SSF56672, SSF56672, 1 hit
    SSF89043, SSF89043, 1 hit
    PROSITEiView protein in PROSITE
    PS51874, PCV_3C_PRO, 1 hit
    PS50507, RDRP_SSRNA_POS, 1 hit
    PS51218, SF3_HELICASE_2, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLG_POL1M
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P03300
    Secondary accession number(s): A0A142KD04
    , P03299, Q84879, Q84880, Q89679
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 7, 2020
    This is version 217 of the entry and version 3 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again